Detergent micelle conjugates containing amino acid monomers allow purification of human IgG near neutral pH

•Aromatic/hydrophobic amino acids are vital additives in antibody purification.•Tyr, Phe, Trp, Ile and Val weaken IgG interaction with Brij-O20 micellar platform.•Phe and Tyr allow recovery at pH 6.3 of ≥ 95% pure IgG with > 80% yield.•IgG recovered at pH6.3 is monomeric independent of the amino acid additive. Industrial scale production of therapeutic monoclonal antibodies (mAbs) is commonly achieved with Protein A chromatography, a process that requires exposure of the antibody to strongly acidic conditions during the eluting step. Exposure to acid inactivates virus contaminants but may, in parallel, lead to antibody aggregation that must be eliminated or kept at acceptably low levels. This report seeks to provide a practical method for overcoming a long-standing problem. We show how Brij-O20 detergent micelles, conjugated by the amphiphilic [(bathophenanthroline)3:Fe2+] complex in the presence of amino acid monomers: phenylalanine (Phe), tyrosine (Tyr), tryptophan (Trp), isoleucine (Ile) or valine (Val), efficiently capture polyclonal human IgG (hIgG) at neutral pH and allow its recovery by extraction either at pH 4 (85–97% yield) or at pH 6.3 (72–84% yield). Of the five amino acid monomers surveyed, Phe or Tyr produced the highest overall process yield at both pH 4 and 6.3. The monomeric state of the purified hIgG's was confirmed by dynamic light scattering (DLS). Potential advantages of the purification method are discussed.